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Chlorine in PDB 7xhr: Crystal Structure of Wild Type Cypovirus Polyhedra Produced By Cell- Free Protein Synthesis

Protein crystallography data

The structure of Crystal Structure of Wild Type Cypovirus Polyhedra Produced By Cell- Free Protein Synthesis, PDB code: 7xhr was solved by S.Abe, J.Tanaka, M.Kojima, K.Hirata, K.Yamashita, T.Ueno, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.30 / 1.80
Space group I 2 3
Cell size a, b, c (Å), α, β, γ (°) 103.61, 103.61, 103.61, 90, 90, 90
R / Rfree (%) 15 / 18.4

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Wild Type Cypovirus Polyhedra Produced By Cell- Free Protein Synthesis (pdb code 7xhr). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Wild Type Cypovirus Polyhedra Produced By Cell- Free Protein Synthesis, PDB code: 7xhr:

Chlorine binding site 1 out of 1 in 7xhr

Go back to Chlorine Binding Sites List in 7xhr
Chlorine binding site 1 out of 1 in the Crystal Structure of Wild Type Cypovirus Polyhedra Produced By Cell- Free Protein Synthesis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Wild Type Cypovirus Polyhedra Produced By Cell- Free Protein Synthesis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl302

b:23.2
occ:1.00
N A:LEU31 3.3 13.1 1.0
CB A:LEU31 3.8 15.0 1.0
CB A:SER30 3.8 12.6 1.0
CG A:LEU31 3.9 15.7 1.0
ND2 A:ASN32 4.1 14.8 1.0
CA A:LEU31 4.1 14.3 1.0
CA A:SER30 4.1 12.8 1.0
C A:SER30 4.2 12.8 1.0
CD1 A:LEU31 4.4 15.3 1.0
OG A:SER30 4.6 12.4 1.0
N A:ASN32 4.6 14.2 1.0
C A:LEU31 4.8 14.4 1.0
CG A:ASN32 4.9 15.2 1.0

Reference:

S.Abe, J.Tanaka, M.Kojima, S.Kanamaru, K.Hirata, K.Yamashita, A.Kobayashi, T.Ueno. Cell-Free Protein Crystallization For Nanocrystal Structure Determination. Sci Rep V. 12 16031 2022.
ISSN: ESSN 2045-2322
PubMed: 36192567
DOI: 10.1038/S41598-022-19681-9
Page generated: Sun Jul 13 08:25:41 2025

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